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Glutathione metabolism and its implications for health
Wu G, Fang YZ, Yang S, Lupton JR & Turner ND
J Nutr. 2004; 134 (3):489-92.
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ABSTRACT
Glutathione ( -glutamyl-cysteinyl-glycine;
GSH) is the most abundant low-molecular-weight thiol, and GSH/glutathione
disulfide is the major redox couple in animal
cells. The synthesis of GSH from glutamate, cysteine, and glycine is
catalyzed sequentially by two cytosolic enzymes, -glutamylcysteine
synthetase and GSH synthetase. Compelling evidence shows that GSH
synthesis is regulated primarily by -glutamylcysteine synthetase activity,
cysteine availability, and GSH feedback inhibition. Animal and human
studies demonstrate that adequate protein nutrition is crucial for the
maintenance of GSH homeostasis. In addition, enteral or parenteral cystine,
methionine, N-acetylcysteine, and L-2-oxothiazolidine-4-carboxylate are
effective precursors of cysteine for tissue GSH synthesis. Glutathione
plays important roles in antioxidant defense, nutrient metabolism, and
regulation of cellular events (including gene expression, DNA and protein
synthesis, cell proliferation and apoptosis, signal transduction, cytokine
production and immune response, and protein glutathionylation).
Glutathione deficiency contributes to oxidative stress, which plays a key
role in aging and the pathogenesis of many diseases (including
kwashiorkor, seizure, Alzheimer’s disease, Parkinson’s disease, liver
disease, cystic fibrosis, sickle cell anemia, HIV, AIDS, cancer, heart
attack, stroke, and diabetes). New knowledge of the nutritional regulation
of GSH metabolism is critical for the development of effective strategies
to improve health and to treat these diseases.
Key Words: amino acids, oxidative stress, cysteine,
disease
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